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"cell loss factor"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
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  • ¿µ¹®
    ÇѱÛ
  • cell membrane permeability
    ¼¼Æ÷¸·Åõ°ú¼º
  • cell organelle
    ¼¼Æ÷¼Ò±â°ü
  • cell respiration
    ¼¼Æ÷È£Èí
  • cell strain
    ¼¼Æ÷ÁÖ
  • cell substitution
    ¼¼Æ÷´ëü, Ç÷±¸´ëü
  • cell surface receptor
    ¼¼Æ÷Ç¥¸é¼ö¿ëü
  • cell swelling
    ¼¼Æ÷Á¾Ã¢
  • cell-associated antibody
    ¼¼Æ÷¿¬°üÇ×ü
  • cell-bound antibody
    ¼¼Æ÷°áÇÕÇ×ü
  • cell-fixed antibody
    ¼¼Æ÷°áÇÕÇ×ü
  • cell-mediated cytolysis
    ¼¼Æ÷¸Å°³¼¼Æ÷¿ëÇØ
  • cell-mediated cytotoxicity
    ¼¼Æ÷¸Å°³¼¼Æ÷µ¶¼º
  • cell-mediated hypersensitivity
    ¼¼Æ÷¸Å°³°ú¹Î¼º
  • cell-mediated immunity
    ¼¼Æ÷¸Å°³¸é¿ª
  • cell-mediated reaction
    ¼¼Æ÷¸Å°³¹ÝÀÀ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 18
  • ¿µ¹®
    ÇѱÛ
  • Chinese hamster ovary cell
    Áß±¹ºñ´ÜÅÐÁã³­¼Ò¼¼Æ÷
  • chromaffin cell
    ģũ·Ò¼¼Æ÷, Å©·Òģȭ¼¼Æ÷
  • chromophilic cell
    »ö¼Òµë¼¼Æ÷, È£»ö¼Ò¼¼Æ÷
  • chromophobic cell
    »ö¼Ò¾Èµë¼¼Æ÷
  • ciliated cell
    ¼¶¸ð¼¼Æ÷, ÀÜÅм¼Æ÷
  • clear cell
    Åõ¸í¼¼Æ÷
  • clear cell carcinoma
    Åõ¸í¼¼Æ÷¾ÏÁ¾
  • clear cell hidradenoma
    Åõ¸í¼¼Æ÷¶¡»ùÁ¾
  • clear cell sarcoma
    Åõ¸í¼¼Æ÷À°Á¾
  • columnar cell
    ¿øÁÖ¼¼Æ÷
  • columnar absorptive cell
    ±âµÕÈíÂø¼¼Æ÷
  • committed cell
    ¾ô¸Ç¼¼Æ÷, ¼öÀÓ¼¼Æ÷
  • complex cell
    º¹ÇÕ¼¼Æ÷
  • cone cell
    ¿ø»Ô¼¼Æ÷
  • cone cell layer
    ¿ø»Ô¼¼Æ÷Ãþ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 18
  • ¿µ¹®
    ÇѱÛ
  • amacrine cell
    ¾Æ¸¶Å©¸° ¼¼Æ÷
  • amacrine cell
    ¹«Ãà»è¼¼Æ÷
  • ameboid cell
    ¾Æ¸Þ¹Ù¸ð¾ç¼¼Æ÷
  • aneuploid cell
    À̼ö¼º¼¼Æ÷
  • anitschkow cell
    ¾Æ´ÏÄ¡ÄÚ¿ì¼¼Æ÷(¡­á¬øà)
  • annular elastotic giant cell granuloma
    ȯ»ó ź·Â ¼¶À¯¼º °Å´ë¼¼Æ÷ À°¾ÆÁ¾
  • anoxic cell
    ¹«»ê¼Ò¼¼Æ÷
  • anti-idiotypic T suppressor cell
    Ç×°³º°Æ¯ÀÌÇü ¾ïÁ¦T¼¼Æ÷
  • antibody dependent cell mediated cytotoxicity
    Ç×üÀÇÁ¸ ¼¼Æ÷¸Å°³ ¼¼Æ÷µ¶¼º.
  • antibody forming cell
    Ç×ü»ý»ê¼¼Æ÷(ù÷ô÷ßæß§á¬øà).
  • antibody producing cell
    Ç×ü»ý»ê¼¼Æ÷
  • antigen presenting cell
    Ç׿øÁ¦½Ã¼¼Æ÷.
  • antigen reactive cell
    Ç׿ø¹ÝÀÀ¼¼Æ÷.
  • apex of cell
    ¼¼Æ÷²À´ë±â
  • apical cell
    Á¤(´Ü)¼¼Æ÷(ð¢Ó®á¬øà)
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  • ¿µ¹®
    ÇѱÛ
  • factor ii(prothrombin)
    Á¦2ÀÎÀÚ(ÇÁ·ÎÆ®·Òºó)
  • factor ix deficiency
    Á¦9ÀÎÀÚ °áÇÌ(Áõ)
  • factor theory
    ¿äÀÎÀÌ·Ð(é©ì×ìµÖå)
  • factor vii
    Á¦7ÀÎÀÚ
  • factor viii deficiency
    Á¦8ÀÎÀÚ °áÇÌ(Áõ)
  • factor viii-vwf complex deficiency
    Á¦8-vWF º¹ÇÕ °áÇÇ
  • factor x
    Á¦10ÀÎÀÚ
  • factor xa
    Á¦10 aÀÎÀÚ
  • factor xiia
    Á¦12 aÀÎÀÚ
  • factor, chemotactic
    È­ÇÐÁÖ¼ºÀÎÀÚ, ÁÖÈ­¼ºÀÎÀÚ
  • factor, macrophage migration inhibition
    ´ë½Ä¼¼Æ÷ À¯ÁÖÀúÁöÀÎÀÚ
  • factor, tumor necrotizing(-sis) (TNF)
    Á¾¾ç±«»çÀÎÀÚ
  • fermentation factor
    ¹ßÈ¿ÀÎÀÚ.
  • fibrin stabilizing factor
    ¼¶À¯¼Ò¾ÈÁ¤ÀÎÀÚ
  • fibrin stabilizing factor =FSF
    ¼¶À¯¼Ò¾ÈÁ¤ÀÎÀÚ(¡­äÌïÒì×í­), ¼¶À¯¼Ò¾ÈÁ¤ÀÎÀÚ.
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 18
  • ¿µ¹®
    ÇѱÛ
  • rho factor
    rho ÀÎÀÚ
  • ribosome dissociating factor
    ¶óÀ̺¸¼Ø ÇØ¸®ÀÎÀÚ(ú°×îì×í­)
  • separation factor
    ºÐ¸®ÀÎÀÚ(ÝÂ×îì×í­)
  • serum prothrombin converting factor
    Ç÷û(úìôè) ÇÁ·ÎÆ®·Òºó ÀüȯÀÎÀÚ(ï®üµì×í­)
  • serum sulfation factor
    Ç÷û À¯È²È­ÀÎÀÚ(úìôè×¼üÜûùì×í­)
  • serum thymic factor
    Ç÷û °©»ó¼±ÀÎÀÚ(úìôèË£ßÒàÍì×í­)
  • sex factor
    ¼ºÀÎÀÚ(àõì×í­)
  • shape factor
    ¸ð¾çÀÎÀÚ(Ù¼åÆì×í­)
  • sigma factor
    ½Ã±×¸¶ÀÎÀÚ(ì×í­)
  • SLR factor
    SLRÀÎÀÚ(ì×í­)
  • somatotropin factor
    ¼Ò¸¶Å䯮·ÎÇÉ ÀÎÀÚ(ì×í­)
  • specificity factor
    ƯÀ̼º ÀÎÀÚ(÷åì¶àõì×í­)
  • spreading factor
    ÆÛÁü ÀÎÀÚ(ì×í­)
  • stable factor
    ¾ÈÁ¤ÀÎÀÚ(äÌïÒì×í­)
  • steric factor
    ÀÔü ÀÎÀÚ(Ø¡ô÷ì×í­)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 18
SHL sensorineural hearing loss
SNHL sensorineural hearing loss
SSNHL sudden sensorineural hearing loss
TEWL transepidermal water loss
TWL transepidermal water loss
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 18
VCAM-1 1/vascular cell adhesion molecule-1
PBSC Peripheral Blood Stem Cell
AC Accessory cell
ACC Acinic cell carcinoma
ALCAM Activated leukocyte cell adhesion molecule
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 18
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • cell substitution
    ¼¼Æ÷ ġȯ, Ç÷±¸ Àç»ý
  • cell surface marker
    ¼¼Æ÷ Ç¥¸é Ç¥ÁöÀÚ
  • cell survival curve
    ¼¼Æ÷ »ýÁ¸ °î¼±
  • cell transfer
    ¼¼Æ÷ ÀÌÀÔ
    Á¼Àº Àǹ̿¡¼­´Â °¢Á¾ ¼¼Æ÷¸¦ ¹æ»ç¼± Á¶»ç µîÀÇ Ã³¸®¸¦ °¡ÇÑ µ¿¹°¿¡ ÁÖÀÔÇϰí ÁÖÀÔµÈ ¼¼Æ÷ÀÇ ¼º»óÀ» Á¶»çÇÏ´Â °ÍÀ» ¸ñÀûÀ¸·Î ÇÑ ¼¼Æ÷ ÁÖÀÔÀÇ ¹æ¹ýÀ» °¡¸®Å°¸ç in vitro¿¡¼­ ¼¼Æ÷ ±â´ÉÀ» Á¶»çÇϱⰡ °ï¶õÇÑ °æ¿ì, in vivo¿¡¼­ÀÇ ¹ÝÀÀ¼ºÀ» Á¶»çÇÏ°í ½ÍÀº °æ¿ì, ¶Ç chimera mouse¸¦ Á¦ÀÛÇÒ ¶§¿¡ »ç¿ëµÈ´Ù. ³ÐÀº Àǹ̿¡¼­´Â ¼¼Æ÷°¡ ÇÑÆí¿¡¼­ ´Ù¸¥ ÆíÀ¸·Î À̵¿ÇÏ´Â °ÍÀ» °¡¸®Å²´Ù.
  • cell typing
    Ç÷±¸Çü °Ë»ç
  • cell wall
    ¼¼Æ÷ º®
    µ¿ÀǾî=cell membrane.
  • cell wall inhibitor
    ¼¼Æ÷ º® ÇÕ¼º ¾ïÁ¦Á¦
  • cell wall teichoic acid
    ¼¼Æ÷ º® ŸÀÌÄÚ»ê
  • cell,hydropic degeneration
    ¼öÆ÷¼º º¯¼º
  • cell-mediated cytotoxicity
    ¼¼Æ÷ ¸Å°³¼º ¼¼Æ÷ µ¶¼º
    Ç×ü ȤÀº lym
  • cell-mediated hypersensitivity
    ¼¼Æ÷ ¸Å°³¼º °ú¹ÎÁõ
    TuberculinÇü Çdz» ¹ÝÀÀÀ» ´ëÇ¥·Î ÇÑ´Ù. ¼¼Æ÷¼º ¸é¿ª ¹ÝÀÀÀÇ ÇÑ ÇüÅÂ. Ç׿ø¿¡ ÀÇÇÏ¿© °¨ÀÛµÈ µ¿¹°ÀÇ Çdz»¿¡ ÀçÂ÷ Ç׿øÀ» ÁÖ»çÇÔÀ¸·Î½á ¼ö ½Ã°£À¸·ÎºÎÅÍ 36½Ã°£ ÈÄ¿¡ ¹ßÀû, °æ°áÀ» ¼ö¹Ý½ÃŰ´Â Á¾Ã¢ÀÌ ÁÖ»ç ºÎÀ§¿¡ ¹ß»ýÇÏ´Â ¹ÝÀÀÀÌ´Ù.
  • cell-mediated immunity
    ¼¼Æ÷ ¸Å°³ ¸é¿ª, ¼¼Æ÷ ¸Å°³¼º ¸é¿ª
  • cell-mediated immunodeficiency syndrome
    ¼¼Æ÷¼º ¸é¿ª °áÇÌ ÁõÈıº
  • central giant cell
    °ñ³» °Å´ë ¼¼Æ÷
  • central giant cell tumor
    Á߽ɼº °Å´ë ¼¼Æ÷ ¾ÏÁ¾
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 18
tissue factor <cell biology> Integral membrane glycoprotein of around 250 residues, that initiates blood clotting after binding factors VII or VIIa.
(18 Nov 1997)
tissue weighting factor In radiation protection, a factor weighting the equivalent dose in a particular tissue or organ in terms of its relative contribution to the total deleterious effects resulting from uniform irradiation of the whole body.
See: effective dose.
(05 Mar 2000)
elongation factor <biochemistry> Peptidyltransferase components of ribosomes that catalyse formation of the acyl bond between the incoming amino acid residue and the peptide chain.
There are three classes of elongation factor: EF1_ (EF Tu in prokaryotes) binds GTP and aminoacyl tRNA, delivering it to the A site of ribosomes. EF 1_ (EF Ts) helps in regeneration of GTP EF 1_. EF 2 (EF G) binds GTP and peptidyl tRNA and translocates it from the A site to the P site. Diptheria toxin inhibits protein synthesis in eukaryotes by adding an ADP ribosyl group to a modified histidine residue (dipthamide) in elongation factor II.
(18 Nov 1997)
transcription factor <molecular biology> Protein required for recognition by RNA polymerases of specific stimulatory sequences in eukaryotic genes.
Several are known that activate transcription by RNA polymerase II when bound to upstream promoters.
Transcription of the 5S RNA gene in Xenopus by RNA polymerase III is dependent on a 40 kD protein TFIIIA that binds to a regulatory site in the centre of the gene and was the first protein found to exhibit the metal binding domains known as zinc fingers.
(17 Mar 1998)
transcription factor ap-1 A multiprotein complex composed of the products of c-jun and c-fos proto-oncogenes. These proteins must dimerise in order to bind to the ap-1 recognition site, also known as the tpa-responsive element (tre). Ap-1 controls both basal and inducible transcription of several genes.
(12 Dec 1998)
transcription factor, sp1 Promoter-specific RNA polymerase II transcription factor that binds to the gc box, one of the upstream promoter elements (upe) in mammalian cells. The binding of sp1 is necessary to initiate transcription in the promoters of a variety of cellular and viral genes including c-ha-ras and HIV.
(12 Dec 1998)
transfer factor A dialysable factor obtained from sensitised T-cells by freezing and thawing, that may possibly immunopotentiate animals.The transfer of specific immunity from one animal to another has been claimed.
(18 Nov 1997)
transforming factor The DNA responsible for bacterial transformation.
(05 Mar 2000)
transforming growth factor <growth factor> Proteins secreted by transformed cells that can stimulate growth of normal cells.
Unfortunate misnomer, since they induce aspects of transformed phenotype, such as growth in semi solid agar, but do not actually transform.
Transforming growth factor alpha, 50 amino acid polypeptide originally isolated from viral transformed rodent cells, contains EGF like domain and binds to EGF receptor. Stimulates growth of microvascular endothelial cells, i.e. Is angiogenic.
Transforming growth factor beta a homodimer of two 112 chains, polypeptide is secreted by many different cell types, stimulates wound healing but in vitro is also a growth inhibitor for certain cell types. The transforming growth factor family includes many of the bone morphogenetic proteins.
Acronym: TGF
(18 Nov 1997)
transforming growth factor alpha Factor isolated in a variety of tissues including epithelium, and maternal decidua. It is closely related to epidermal growth factor (epidermal growth factor-urogasterone) and binds to the egf receptor. Tgf-alpha acts synergistically with tgf-beta in inducing phenotypic transformation, but its physiological role is unknown.
(12 Dec 1998)
transforming growth factor beta Factor synthesised in a wide variety of tissues including platelets, placenta, and both normal and transformed cell lines. It acts synergistically with tgf-alpha in inducing phenotypic transformation and can also act as a negative autocrine growth factor. Tgf-beta also has a potential role in embryonal development, cellular differentiation, hormone secretion, and immune function. There are at least three forms of tgf-beta: tgf-beta1, tgf-beta2, and tgf-beta1.2. The latter is a heterodimer made up of both tgf-beta1 and tgf-beta2.
(12 Dec 1998)
transmethylation factor <biochemistry> Esterified in the head group of phospholipids (phosphatidylcholine and sphingomyelin) and in the neurotransmitter acetylcholine. Otherwise a biological source of methyl groups.
(18 Nov 1997)
endothelial relaxing factor A molecule functioning as a neurotransmitter and produced by activated macrophages. It is capable of killing tumour cells, parasites, and intracellular bacteria.
(05 Mar 2000)
endothelium-derived growth factor synthase <enzyme> Converts l-arginine to a smooth muscle relaxing factor and stimulates the formation of cyclic-GMP
Registry number: EC 1.5.1.-
Synonym: edrf synthase
(26 Jun 1999)
endothelium derived relaxation factor <biochemistry> This compound is produced from L arginine by the enzyme nitric oxide synthase. Acts as a potent vasorelaxant via elevation of intracellular cGMP in vascular smooth muscle.
Synthesis of nitric oxide is not confined to endothelium, isoforms of nitric oxide synthase are also found in brain, neutrophils and platelets.
Synonym: endothelium derived relaxation factor.
Acronym: NO
(29 Dec 1997)
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